(data stored in ACNUC16935 zone)

SWISSPROT: C8VLL2_EMENI

ID   C8VLL2_EMENI            Unreviewed;       565 AA.
AC   C8VLL2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 44.
DE   RecName: Full=Arylsulfatase {ECO:0000256|PIRNR:PIRNR000972};
DE            Short=AS {ECO:0000256|PIRNR:PIRNR000972};
DE            EC=3.1.6.1 {ECO:0000256|PIRNR:PIRNR000972};
DE   AltName: Full=Aryl-sulfate sulphohydrolase {ECO:0000256|PIRNR:PIRNR000972};
GN   ORFNames=ANIA_11149 {ECO:0000313|EMBL:CBF84693.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84693.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY: A phenol sulfate + H(2)O = a phenol + sulfate.
CC       {ECO:0000256|PIRNR:PIRNR000972}.
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-
CC       formylglycine, FGly), of a serine or cysteine residue in
CC       prokaryotes and of a cysteine residue in eukaryotes, is critical
CC       for catalytic activity. {ECO:0000256|PIRSR:PIRSR000972-50}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|PIRNR:PIRNR000972}.
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DR   EMBL; BN001307; CBF84693.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8VLL2; -.
DR   STRING; 162425.CADANIAP00007963; -.
DR   EnsemblFungi; CADANIAT00007963; CADANIAP00007963; CADANIAG00007963.
DR   HOGENOM; HOG000169239; -.
DR   InParanoid; C8VLL2; -.
DR   OMA; CEFADSE; -.
DR   OrthoDB; EOG092C1Z5S; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR012083; Arylsulfatase.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF000972; Arylsulf_plant; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VLL2.
DR   SWISS-2DPAGE; C8VLL2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    565       Arylsulfatase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002991615.
FT   DOMAIN       24    370       Sulfatase. {ECO:0000259|Pfam:PF00884}.
FT   MOD_RES      68     68       3-oxoalanine (Cys). {ECO:0000256|PIRSR:
FT                                PIRSR000972-50}.
SQ   SEQUENCE   565 AA;  64167 MW;  9D976CA440116772 CRC64;
     MKLSSLVALV GVSALSEASP RPKPNFVFVF TDDQDLTMNS VEYMPHVAGR IRDRGLDFTN
     HFVTTALCCP SRVSLWTGRQ AHNTNVTWVA PPYGGYPKFV SQGFNEDWFP LWLQDAGYNT
     YYVGKLFNAH SVTTYNNPFV KGFNGSDFLL DPFTYSYWNS SYQRNHEAPK SYAGQYTTDV
     TEEKALGFVD DALEDKERPF FLTVAPIAPH FEQDPGHSSD TPPQAPIPAP RHAHLFPDAK
     VPRVPSFNPL NQTGPSWIRD LKHQNQSVVD YEDFFYRQRL RALQSVDEMV DKLLDRLERS
     GQLNNTYVIY SSDNGFHIGH HRLPPGKSTS YEEDIRVPFF IRGPGIKSGG KVTQVTTHID
     FAPTIFELLG LPPRSDFDGT PMRIMKDSAA IPHEHVIVEY WGQALMMVTA PTNTDRMPNT
     TYKSVRLLSE KYNLFYAVWC TGDHELFDLN TDPYQMHNIY NTASRSFKNR LDALLLVLKS
     CAGSTCIKPW AELHPDGSVQ SLSDALDSQY DGFYAQLPKV EYEACVDGYL IAAEGLQWED
     VSASALRNYV RRNYAFDDVQ KYRKL
//

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